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Biomedical subjects

J E Paciga

Publications and source records attributed to J E Paciga.

24 records · Page 2Linked to original sources
PubMed1979

Sequential changes of surfactant phosphatidylcholine in hyaline-membrane disease of the newborn.

Although reduced levels of lung surfactant are known to predispose to hyaline-membrane disease, the role of biochemical changes in surfactant composition has not been defined. We found that surfactant isolated from pharyngeal and tracheal aspirates of newborns with hyaline-membrane disease had a distinctly different phosphatidylcholine fatty acid composition from surfactant of control infants. Surfactant phosphatidylcholine from newborns with hyaline-membrane disease had a lower percentage of palmitic acid and higher percentages of the 18-carbon and 20-carbon fatty acids, irrespective of gestational age. Evaluation of serial aspirates for 18 days revealed that in hyaline-membrane disease the surfactant phosphatidylcholine fatty acids followed a predictable pattern of change, gradually becoming similar to those of the control group. Evaluation of surfactant from tracheal and pharyngeal aspirates effectively monitors the biochemical maturation of the surfactant system in hyaline-membrane disease.

Age Factors↗
PubMed1977

Isolation and characterization of proteins associated with the lung surfactant system.

Rabbit lung washings and purified lung surfactant were delipidated without precipitation or loss of protein. This enabled effective study of the proteins by electrophoretic and immunoelectrophoretic techniques. The lung washings contained secretory immunoglobulin A and several serum proteins. The protein composition of purified lung surfactant was the same as the unfractionated lung washings confirming our previous study which indicated that there is no specific protein associated with surfactant phospholipids obtained by alveolar lavage with isotonic saline.

Animals↗
PubMedDate not supplied

Lung surfactant-associated glycoproteins and proteolipids in human amniotic fluids evaluated by dot immunobinding assays.

Dot immunobinding assays for the quantitation of two classes of proteins associated with lung surfactant phospholipids in human amniotic fluid are described. With the use of these assays it was determined that the two classes of surfactant proteins accumulate in the amniotic fluid at the same rate. The concentrations of disaturated phosphatidylcholine and the surfactant-associated proteins are less closely correlated. Centrifugation of amniotic fluids either before or after freezing resulted in a loss ranging from 10 to 35 percent of both surfactant disaturated phosphatidylcholine and proteins depending on the relative centrifugal force used. Preterm amniotic fluids contained significantly less of both surfactant-associated proteins, as well as disaturated phosphatidylcholine, than did term amniotic fluids which suggests that the use of these specific protein markers may enhance the assessment of fetal lung maturity.

Amniotic Fluid↗